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Division of Molecular Pharmacology, Departments of Pharmacology and
Psychiatry, MCP-Hahnemann School of Medicine, Philadelphia,
Pennsylvania 19129 (E.F., L.-Q.J., G.-P.C., H.-Y.W.),
Experimental
Therapeutics Branch, National Institute of Neurological Disorders and
Stroke, National Institutes of Health, Bethesda, Maryland 20892 (T.R.H., D.R.S.), and
Department of Anatomy, Monash University,
Clayton, Victoria, Australia (J.D.)
Accumulated evidence suggests that dopamine and dopamine D1
agonists can activate phospholipase C in both brain and peripheral tissue. The receptor that mediates the hydrolysis of phosphoinositides has not been identified. The cloned dopamine D1A receptor
that is generally thought to be linked to adenylyl cyclase, has also been proposed to couple to phospholipase C. However, a number of
studies have suggested that this signaling pathway is mediated via a
distinct D1-like dopamine receptor. We tested whether the D1A site plays a role in stimulating phosphoinositide
hydrolysis by using the dopamine D1A-deficient mutant mice
as a test model. Results show that although D1 dopamine
receptor-mediated production of cAMP is completely absent in membranes
of D1A-deficient mice, D1 receptor-mediated
accumulation of inositol phosphate is identical in tissues of mutant
and wild-type animals. Furthermore, the coupling of
[3H]SCH23390 binding sites in striatal or frontal cortex
membranes to G
s is markedly reduced, although coupling
of [3H]SCH23390 binding sites to Gq was
unaltered in tissue taken from D1A mutant mice compared
with control animals. These results clearly demonstrate that
dopaminergic stimulation of inositol phosphate formation is mediated by
a D1 dopamine receptor subtype that is distinct from the
D1A receptor that activates adenylyl cyclase.
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